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Journal articles on the topic 'Horse, selenium, glutathione peroxidase'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Robbins, Charles T., Steven M. Parish, and Barbara L. Robbins. "Selenium and glutathione peroxidase activity in mountain goats." Canadian Journal of Zoology 63, no. 7 (1985): 1544–47. http://dx.doi.org/10.1139/z85-229.

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Blood glutathione peroxidase (GSH-Px) activity in mountain goats (Oreamnos americanus) is a linear function of blood selenium. GSH-Px activity per unit of selenium (Se) in mountain goats is approximately double that published for the domestic cow and horse. It is hypothesized that high GSH-Px activity per unit selenium in mountain goats reduces their dietary selenium requirement relative to the above domestic species and is an essential adaptation for occupying low-selenium environments. GSH-Px activity peaked 20–30 days after injections of 0.1 and 0.3 mg Se/kg. A higher dose of 0.5 mg Se/kg d

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2

Pilarczyk, B., A. Tomza-Marciniak, T. Stankiewicz, et al. "Serum selenium concentration and glutathione peroxidase activity and selenium content in testes of Polish Konik horses from selenium- -deficient area in North-Western Poland." Polish Journal of Veterinary Sciences 17, no. 1 (2014): 165–67. http://dx.doi.org/10.2478/pjvs-2014-0022.

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Abstract The aim of this study was to determine serum selenium concentrations in Polish Konik horses residing in the Odra Delta Nature Park (Poland) and to evaluate the activity of glutathione peroxidase and Se content in testes of this horse breed. In over 95% of cases, serum Se concentration was below the optimal range, and none of the horses examined was deficient in this trace element. The lack of Se deficiency in the animals examined suggests however, that the Polish Konik horses have a natural ability to the optimal use of nutrients available in their life area. Testicular content of Se

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3

Shellow, J. S., S. G. Jackson, J. P. Baker, and A. H. Cantor. "The Influence of Dietary Selenium Levels on Blood Levels of Selenium and Glutathione Peroxidase Activity in the Horse." Journal of Animal Science 61, no. 3 (1985): 590–94. http://dx.doi.org/10.2527/jas1985.613590x.

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4

Ludvikova, E., P. Jahn, and Z. Lukas. "Nutritional myodegeneration as a cause of dysphagia in adult horses: three case reports." Veterinární Medicína 52, No. 6 (2008): 267–72. http://dx.doi.org/10.17221/1880-vetmed.

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Three cases of nutritional myodegeneration caused by selenium deficiency in adult horses are described. Difficulty in eating and drinking was a common clinical sign in all horses. Blood biochemistry revealed a marked elevation of muscle enzymes and low glutathione peroxidase activity or low selenium concentration in whole blood in all cases. The treatment with sodium selenite and vitamin E was instituted in all horses. Two of them were euthanized because of continuing muscle injuries, one patient was cured. The post-mortem examination of euthanized horses revealed pale muscles that were distri

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5

de Moffarts, Brieuc, Nathalie Kirschvink, Emmanuelle van Erck, Tatiana Art, Joël Pincemail, and Pierre Lekeux. "Assessment of the oxidant–antioxidant blood balance in a field exercise test in Standardbredand eventing horses." Equine and Comparative Exercise Physiology 2, no. 4 (2005): 253–61. http://dx.doi.org/10.1079/ecp200567.

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AbstractThe aim of this study was to determine which oxidant–antioxidant blood markers are of interest for a field exercise test (ET) performed on a racetrack. Healthy Standardbred horses (S: n = 12) and healthy eventing horses (E: n=12) were investigated. Exercise was monitored by measuring velocity (V), heart rate (HR), and plasma lactate (LA). Whilst maximal LA did not differ (11.8±0.88 mmol l−1), maximal V (S: 12.3±0.17 m s−1versus E: 11.1±0.24 m s−1, P<0.05) and final HR (S: 222±1 versus E: 203±8 beats min−1, P<0.05) were significantly different between groups. Venous blood was coll

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6

Calamari, L., Piccioli Cappelli, A. Ferrari, and G. Bertin. "Glutathione peroxidase responses in mature horses following the withdrawal of an organic selenium supplement." Italian Journal of Animal Science 6, sup1 (2007): 275–77. http://dx.doi.org/10.4081/ijas.2007.1s.275.

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7

Cantón, E. Velázquez, A. H. Ramírez Pérez, L. A. Zarco Quintero, R. Rosiles Martínez, and J. C. Ángeles Hernández. "0818 Effect of selenium and vitamin E supplementation on blood glutathione peroxidase activity and selenium in moderately exercised horses." Journal of Animal Science 94, suppl_5 (2016): 393–94. http://dx.doi.org/10.2527/jam2016-0818.

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8

Brummer, M., S. Hayes, B. E. Harlow, et al. "Effect of selenium status on the response of unfit horses to exercise." Comparative Exercise Physiology 8, no. 3-4 (2012): 203–12. http://dx.doi.org/10.3920/cep12022.

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Exercise is known to increase reactive oxygen species and alter glutathione peroxidase activity (GPx), a selenoenzyme responsible for neutralising hydrogen peroxide. This study evaluated the effect of selenium (Se) status on the response of unfit horses to mild exercise. 25 mature horses received one of four dietary treatments for 29 weeks: low Se (LS, n=6), adequate Se (AS, sodium selenite, n=6), high organic Se (SP; Sel-Plex®, n=7) or high inorganic Se (SS, sodium selenite, n=6). Total dietary Se concentration for LS, AS, SP and SS was 0.06, 0.12, 0.3 and 0.3 mg/kg respectively. Blood sample

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9

Avissar, N., J. C. Whitin, P. Z. Allen, D. D. Wagner, P. Liegey, and H. J. Cohen. "Plasma Selenium-dependent Glutathione Peroxidase." Journal of Biological Chemistry 264, no. 27 (1989): 15850–55. http://dx.doi.org/10.1016/s0021-9258(18)71555-x.

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10

Beasley, R., C. Thomson, and N. Pearce. "Selenium, glutathione peroxidase and asthma." Clinical Experimental Allergy 21, no. 2 (1991): 157–59. http://dx.doi.org/10.1111/j.1365-2222.1991.tb00824.x.

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11

TARP, U. "Selenium Glutathione Peroxidase in Rheumatoid Arthritis." Rheumatology 29, no. 2 (1990): 158. http://dx.doi.org/10.1093/rheumatology/29.2.158-a.

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12

Sunde, Roger A. "Selenium status regulates glutathione peroxidase expression." Journal of Inorganic Biochemistry 43, no. 2-3 (1991): 283. http://dx.doi.org/10.1016/0162-0134(91)84272-b.

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13

Burk, R. F., K. E. Hill, R. Read, and T. Bellew. "Response of rat selenoprotein P to selenium administration and fate of its selenium." American Journal of Physiology-Endocrinology and Metabolism 261, no. 1 (1991): E26—E30. http://dx.doi.org/10.1152/ajpendo.1991.261.1.e26.

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Selenoprotein P is a glycoprotein that contains greater than 60% of the selenium in rat plasma. Physiological experiments were undertaken to gain insight into selenoprotein P function. Selenium-deficient rats were injected with doses of selenium ranging from 25 to 200 micrograms/kg, and the appearance of selenoprotein P was compared with the appearance of glutathione peroxidase activity in plasma and in liver. Selenoprotein P concentration increased to 35% of control by 6 h, whereas glutathione peroxidase activity increased minimally or not at all. Moreover, in rats given 100 and 200 microgram

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14

Lloyd, B., E. Robson, I. Smith, and B. E. Clayton. "Blood selenium concentrations and glutathione peroxidase activity." Archives of Disease in Childhood 64, no. 3 (1989): 352–56. http://dx.doi.org/10.1136/adc.64.3.352.

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15

Mishra, Prafulla Kumar, and J. Chaudhuri. "Blood glutathione peroxidase and selenium in abortion." Indian Journal of Clinical Biochemistry 18, no. 1 (2003): 96–98. http://dx.doi.org/10.1007/bf02867673.

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16

Kirana, Annisa Nurul, Erfi Prafiantini, and Novi Silvia Hardiany. "Correlation Between Age, Body Mass Index, And Blood Selenium Level with Glutathione Peroxidase Activity Among Elderly in South Jakarta." International Journal of Human and Health Sciences (IJHHS) 4, no. 2 (2020): 89. http://dx.doi.org/10.31344/ijhhs.v4i2.181.

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Oxidative stress contributed in aging process and several degenerative diseases. Selenium was an important trace element due to as a component of antioxidants enzymes (selenoproteins), including glutathione peroxidase for protection against free radical.Objective: We aimed to study the correlation between blood selenium level and plasma glutathione peroxidase activity in elderly.Materials and Methods: Cross sectional study was held in 5 elderly communities in south Jakarta. Body mass index, blood selenium level and plasma glutathione peroxidase activity were measured in 95 elderly aged between

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17

Lang, J. K., K. Gohil, L. Packer, and R. F. Burk. "Selenium deficiency, endurance exercise capacity, and antioxidant status in rats." Journal of Applied Physiology 63, no. 6 (1987): 2532–35. http://dx.doi.org/10.1152/jappl.1987.63.6.2532.

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Increased O2 metabolism imposed by physical exercise is likely to augment the production of active O2 species that have been shown to react with lipids, proteins, and DNA. Antioxidants and antioxidant enzymes, such as the selenium enzyme glutathione peroxidase, minimize or prevent such potentially toxic reactions. This study shows that selenium deficiency decreases glutathione peroxidase activity in liver and muscle (less than 80%, P less than 0.001), increases total glutathione in liver, muscle, and plasma (P less than 0.05) and increases muscle cytochrome oxidase activity, and ubiquinone con

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18

Björkman, Lars, Magnus Svartengren, and Monica Nordberg. "Individual Differences in Activity of Glutathione Peroxidase and Catalase Studied in Monozygotic Twins Discordant for Smoking." Human & Experimental Toxicology 11, no. 5 (1992): 341–46. http://dx.doi.org/10.1177/096032719201100507.

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1 Cigarette smoke contains free radicals. The enzymes glutathione peroxidase (GSH-px) and catalase are important parts of the anti-oxidative protecting system. 2 Ten pairs of monozygotic twins, who were discordant for smoking, were analysed in order to determine their erythrocyte glutathione peroxidase and catalase activities and their plasma concentrations of selenium. 3 Analysis of variance (ANOVA) revealed that the difference in activities of catalase and glutathione peroxidase was much less within pairs than between pairs, indicating a large individual variation due to genetic expression o

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19

Steinberg, P., H. Schramm, L. Schladt, L. W. Robertson, H. Thomas, and F. Oesch. "The distribution, induction and isoenzyme profile of glutathione S-transferase and glutathione peroxidase in isolated rat liver parenchymal, Kupffer and endothelial cells." Biochemical Journal 264, no. 3 (1989): 737–44. http://dx.doi.org/10.1042/bj2640737.

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The distribution and inducibility of cytosolic glutathione S-transferase (EC 2.5.1.18) and glutathione peroxidase (EC 1.11.1.19) activities in rat liver parenchymal, Kupffer and endothelial cells were studied. In untreated rats glutathione S-transferase activity with 1-chloro-2,4-dinitrobenzene and 4-hydroxynon-2-trans-enal as substrates was 1.7-2.2-fold higher in parenchymal cells than in Kupffer and endothelial cells, whereas total, selenium-dependent and non-selenium-dependent glutathione peroxidase activities were similar in all three cell types. Glutathione S-transferase isoenzymes in par

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20

Cser, M. À., I. Sziklai-László, H. Menzel, and I. Lombeck. "Selenium and Glutathione Peroxidase Activity in Hungarian Children." Journal of Trace Elements in Medicine and Biology 10, no. 3 (1996): 167–73. http://dx.doi.org/10.1016/s0946-672x(96)80028-9.

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21

Bartfay, Wally J., and Emma Bartfay. "Selenium and Glutathione Peroxidase With Beta-Thalassemia Major." Nursing Research 50, no. 3 (2001): 178–83. http://dx.doi.org/10.1097/00006199-200105000-00009.

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22

Molin, Margareta, Stefan L. Marklund, Bo Bergman, and Bo Nilsson. "Mercury, selenium, and glutathione peroxidase in dental personnel." Acta Odontologica Scandinavica 47, no. 6 (1989): 383–90. http://dx.doi.org/10.3109/00016358909004807.

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23

Zhang, Zhenhua, Shin-Ichi Miyatake, Masaaki Saiki, et al. "Selenium and Glutathione Peroxidase mRNA in Rat Glioma." Biological Trace Element Research 73, no. 1 (2000): 67–76. http://dx.doi.org/10.1385/bter:73:1:67.

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24

Wang, Yong Xian, and Josef Kiem. "Effect of selenium supplementation on platelet selenium, glutathione peroxidase, and aggregation." Biological Trace Element Research 15, no. 1 (1988): 89–96. http://dx.doi.org/10.1007/bf02990128.

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25

BERMANO, Giovanna, John R. ARTHUR, and John E. HESKETH. "Role of the 3′ untranslated region in the regulation of cytosolic glutathione peroxidase and phospholipid-hydroperoxide glutathione peroxidase gene expression by selenium supply." Biochemical Journal 320, no. 3 (1996): 891–95. http://dx.doi.org/10.1042/bj3200891.

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Selenium is an essential nutrient and synthesis of selenoproteins is affected by limited selenium supply. During selenium deficiency there is a differential regulation of selenoprotein synthesis and gene expression; for example, there is a decrease in abundance of mRNA for cytosolic glutathione peroxidase (cGSH-Px) and a preservation of mRNA for phospholipid-hydroperoxide glutathione peroxidase (PHGSH-Px). This difference is not due to an alteration in the rate of transcription but might reflect differences in translation. The aim of the present work was to assess the role of cGSH-Px and PHGSH

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26

Czuczejko, Jolanta, Bronisław A. Zachara, Ewa Staubach-Topczewska, Waldemar Halota, and Józef Kedziora. "Selenium, glutathione and glutathione peroxidases in blood of patients with chronic liver diseases." Acta Biochimica Polonica 50, no. 4 (2003): 1147–54. http://dx.doi.org/10.18388/abp.2003_3638.

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Disturbances in the antioxidant system could play a role in pathogenesis of chronic liver disease. The aim of our study was to evaluate the levels/activities of antioxidants in blood of patients with chronic liver disease. We estimated selenium and glutathione concentrations and glutathione peroxidase activities in blood of 59 patients with chronic hepatitis B or C virus infection (group 1) and 64 patients with alcoholic, autoimmune or cryptogenic chronic liver disease (group 2). The results were compared with 50 healthy controls. Whole blood and plasma selenium and red cell glutathione concen

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27

Weiss, Sherri L., Jacqueline K. Evenson, Kevin M. Thompson, and Roger A. Sunde. "The Selenium Requirement for Glutathione Peroxidase mRNA Level Is Half of the Selenium Requirement for Glutathione Peroxidase Activity in Female Rats." Journal of Nutrition 126, no. 9 (1996): 2260–67. http://dx.doi.org/10.1093/jn/126.9.2260.

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28

Bermano, Giovanna, John R. Arthur, and John E. Hesketh. "Selective control of cytosolic glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase mRNA stability by selenium supply." FEBS Letters 387, no. 2-3 (1996): 157–60. http://dx.doi.org/10.1016/0014-5793(96)00493-0.

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29

McMaster, D., N. Bell, P. Anderson, and A. H. Love. "Automated measurement of two indicators of human selenium status, and applicability to population studies." Clinical Chemistry 36, no. 2 (1990): 211–16. http://dx.doi.org/10.1093/clinchem/36.2.211.

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Abstract We developed an automated system consisting of a centrifugal analyzer and an atomic absorption spectrophotometer with Zeeman background correction to produce a profile of the concentrations of selenium and the selenium-dependent enzyme glutathione peroxidase (EC 1.11.1.9) in serum and whole blood, for use in epidemiological surveys in Northern Ireland. No pretreatment of samples other than dilution is required, and at least 35 subjects can be screened within 24 h of venesection. For selenium in serum the between-run CV was 5.7% and 4.4% within run. For selenium in whole blood the CV w

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30

Zhu, Zongjian, Mieko Kimura, and Yoshinori Itokawa. "Selenium concentration and glutathione peroxidase activity in selenium and magnesium deficient rats." Biological Trace Element Research 37, no. 2-3 (1993): 209–17. http://dx.doi.org/10.1007/bf02783796.

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31

Huang, Yi, Dan-Yang Ge, Hui Zong, Ju-Xin Yin, Xiao-Nan Qu, and Shao-Wu Lv. "Active Site Mimicry of Glutathione Peroxidase by Glutathione Imprinted Selenium-Containing Trypsin." Catalysts 7, no. 10 (2017): 282. http://dx.doi.org/10.3390/catal7100282.

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32

Yu, Huijun, Junqiu Liu, Xiaoman Liu, Tianzhu Zang, Guimin Luo, and Jiacong Shen. "Kinetic studies on the glutathione peroxidase activity of selenium-containing glutathione transferase." Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 141, no. 3 (2005): 382–89. http://dx.doi.org/10.1016/j.cbpc.2005.05.003.

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33

Kim, Hyun-Ha, Hye-Ran Yang, and Hye-Young P. Kim. "Selenium Status and Glutathione Peroxidase Activity in Korean Infants." Korean Journal of Nutrition 44, no. 2 (2011): 112. http://dx.doi.org/10.4163/kjn.2011.44.2.112.

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34

Fisher, Aron B., Chandra Dodia, Yefim Manevich, Jin-Wen Chen, and Sheldon I. Feinstein. "Phospholipid Hydroperoxides Are Substrates for Non-selenium Glutathione Peroxidase." Journal of Biological Chemistry 274, no. 30 (1999): 21326–34. http://dx.doi.org/10.1074/jbc.274.30.21326.

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35

Christensen, Merrill J., and Kenneth W. Burgener. "Dietary Selenium Stabilizes Glutathione Peroxidase mRNA in Rat Liver." Journal of Nutrition 122, no. 8 (1992): 1620–26. http://dx.doi.org/10.1093/jn/122.8.1620.

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36

Tubman, T. R. J., H. L. Halliday, and D. McMaster. "Glutathione Peroxidase and Selenium Levels in the Preterm Infant." Neonatology 58, no. 6 (1990): 305–10. http://dx.doi.org/10.1159/000243284.

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37

Natta, C. L., L. C. Chen, and C. K. Chow. "Selenium and Glutathione Peroxidase Levels in Sickle Cell Anemia." Acta Haematologica 83, no. 3 (1990): 130–32. http://dx.doi.org/10.1159/000205188.

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38

Coakley, JH, MJ Stokes, O. Oster, RHT Edwards, and MJ Jackson. "Glutathione Peroxidase Activity and Selenium Therapy in Muscular Dystrophies." Clinical Science 75, s19 (1988): 40P. http://dx.doi.org/10.1042/cs075040pb.

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39

Zhang, W., C. S. Ramanathan, R. G. Nadimpalli, A. A. Bhat, A. G. Cox, and E. W. Taylor. "Selenium-dependent glutathione peroxidase modules encoded by RNA viruses." Biological Trace Element Research 70, no. 2 (1999): 97–116. http://dx.doi.org/10.1007/bf02783852.

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40

Paszkowski, T., A. I. Traub, S. Y. Robinson, and D. McMaster. "Selenium dependent glutathione peroxidase activity in human follicular fluid." Clinica Chimica Acta 236, no. 2 (1995): 173–80. http://dx.doi.org/10.1016/0009-8981(95)98130-9.

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41

Silva, Neyla Edelwais, Cervantes Caporossi, Alberto Bicudo Salomão, Diana Borges Dock Nascimento, and Daniela Alencar Moreira. "Avaliação dos níveis de selênio e glutationa peroxidase em pacientes críticos." Braspen Journal 35, no. 3 (2020): 222–29. http://dx.doi.org/10.37111/braspenj.2020353005.

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Introduction: The ability of selenium to reduce free radicals, associated with its performance as an essential cofactor for glutathione peroxidase, confers a potential role for patients in the intensive care unit. The aim of this study was to evaluate the plasma levels of selenium and glutathione peroxidase at admission and for the period of 7 days of evolution in hospitalized patients. Methods: Observational study with adult patients (n = 22) admitted to the intensive care unit. Three blood samples were taken, on days 1, 3 and 7, to assess selenium, and two for glutathione peroxidase, on days

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42

George, Joseph. "Determination of selenium during pathogenesis of hepatic fibrosis employing hydride generation and inductively coupled plasma mass spectrometry." Biological Chemistry 399, no. 5 (2018): 499–509. http://dx.doi.org/10.1515/hsz-2017-0260.

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Abstract Serum and liver selenium levels were studied during the pathogenesis of N-nitrosodimethylamine (NDMA) induced hepatic fibrosis in rats. The degree of fibrosis was assessed with Masson’s trichrome staining and quantifying collagen content in the liver. Lipid peroxides were measured in blood and liver samples and total glutathione and glutathione peroxidase were assayed in the liver tissue to evaluate oxidative stress. Interleukin-6 (IL-6) and transforming growth factor-β1 (TGF-β1) were measured in the serum. Selenium levels were determined using inductively coupled plasma-mass spectrom

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43

Shigeoka, S., T. Takeda, and T. Hanaoka. "Characterization and immunological properties of selenium-containing glutathione peroxidase induced by selenite in Chlamydomonas reinhardtii." Biochemical Journal 275, no. 3 (1991): 623–27. http://dx.doi.org/10.1042/bj2750623.

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The selenite-induced glutathione peroxidase in Chlamydomonas reinhardtii has been purified about 323-fold with a 10% yield, as judged by PAGE. The native enzyme had an Mr of 67,000 and was composed of four identical subunits of Mr 17,000. Glutathione was the only electron donor, giving a specific activity of 193.6 mumol/min per mg of protein. L-Ascorbate, NADH, NADPH, pyrogallol, guaiacol and o-dianisidine did not donate electrons to the enzyme. In addition to H2O2, organic hydroperoxides were reduced by the enzyme. The Km values for glutathione and H2O2 were 3.7 mM and 0.24 mM respectively. T

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44

Tahmasbi, Davoud, Saeid Gorgin, Mohammad Mazendarani, and Mohammad Sudagar. "Effect of vitamin E (DL-all-rac-a-tocopherol acetate) and nano particles of selenium on growth, survival, body composition and whole body glutathione peroxidase (GPX) and malondialdehyde (MDA) in Rutilus kutum (Kamensky, 1901)." Transylvanian Review of Systematical and Ecological Research 19, no. 2 (2017): 69–76. http://dx.doi.org/10.1515/trser-2017-0014.

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Abstract The effect of vitamin E (100 mg kg−1) and nano-selenium (1 mg kg−1), which have a nutritional relationship separately and in combination, was investigated on growth, survival, carcass composition, body glutathione peroxidase activity, and body malondialdehyde content of Rutilus kutum. Results showed that vitamin E is capable of improving growth, FCR and WG in Kutum fingerlings; however, nano-selenium is not. According to this study, vitamin E can improve growth and selenium can improve glutathione peroxidase activity in Rutilus kutum larvae.

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45

Olson, Gary E., John C. Whitin, Kristina E. Hill, et al. "Extracellular glutathione peroxidase (Gpx3) binds specifically to basement membranes of mouse renal cortex tubule cells." American Journal of Physiology-Renal Physiology 298, no. 5 (2010): F1244—F1253. http://dx.doi.org/10.1152/ajprenal.00662.2009.

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Glutathione peroxidase-3 (Gpx3), also known as plasma or extracellular glutathione peroxidase, is a selenoprotein secreted primarily by kidney proximal convoluted tubule cells. In this study Gpx3−/−mice have been produced and immunocytochemical techniques have been developed to investigate Gpx3 metabolism. Gpx3−/−mice maintained the same whole-body content and urinary excretion of selenium as did Gpx3+/+mice. They tolerated selenium deficiency without observable ill effects. The simultaneous knockout of Gpx3 and selenoprotein P revealed that these two selenoproteins account for >97% of plas

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46

Baliga, R., M. Baliga, and S. V. Shah. "Effect of selenium-deficient diet in experimental glomerular disease." American Journal of Physiology-Renal Physiology 263, no. 1 (1992): F56—F61. http://dx.doi.org/10.1152/ajprenal.1992.263.1.f56.

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We examined the effect of a selenium-deficient diet on two experimental models of glomerular disease, the puromycin aminonucleoside (PAN)-induced nephrotic syndrome, a model of minimal change disease, and passive Heymann nephritis, a complement-dependent and neutrophil-independent model that resembles membranous nephropathy. The specific activity of selenium-dependent glutathione peroxidase was markedly reduced in the liver, the kidney cortex, and in glomeruli in weanling male Sprague-Dawley rats placed on a selenium-deficient diet for 6 wk compared with rats fed a selenium-replete diet, with

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47

Girelli, Domenico, Oliviero Olivieri, Anna Maria Stanzial, et al. "Low Platelet Glutathione Peroxidase Activity and Serum Selenium Concentration in Patients with Chronic Renal Failure: Relations to Dialysis Treatments, Diet and Cardiovascular Complications." Clinical Science 84, no. 6 (1993): 611–17. http://dx.doi.org/10.1042/cs0840611.

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1. Selenium status was investigated in patients with chronic renal failure, with special regard to its relations to the dialysis treatments, dietary habits and clinical signs of atherosclerosis. 2. Serum selenium concentration and platelet glutathione peroxidase activity were measured in 45 patients with chronic renal failure subdivided into three groups according to the type of treatment: 15 non-dialysed, 15 on haemodialysis, 15 on continuous ambulatory peritoneal dialysis. A 7-day diet history was carried out in all patients. Seventeen of the patients with chronic renal failure had clinicall

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48

Li, N. Q., P. S. Reddy, K. Thyagaraju, et al. "Elevation of rat liver mRNA for selenium-dependent glutathione peroxidase by selenium deficiency." Journal of Biological Chemistry 265, no. 1 (1990): 108–13. http://dx.doi.org/10.1016/s0021-9258(19)40202-0.

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49

Zhu, Zongjian, Mieko Kimura, and Yoshinori Itokawa. "Effect of selenium and protein deficiency on selenium and glutathione peroxidase in rats." Biological Trace Element Research 36, no. 1 (1993): 15–23. http://dx.doi.org/10.1007/bf02783776.

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Chang, Mei, and C. Channa Reddy. "Active transcription of the selenium-dependent glutathione peroxidase gene in selenium-deficient rats." Biochemical and Biophysical Research Communications 181, no. 3 (1991): 1431–36. http://dx.doi.org/10.1016/0006-291x(91)92099-6.

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